期刊
BIOLOGICAL CHEMISTRY
卷 391, 期 5, 页码 581-587出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2010.055
关键词
cancer; matrix metalloproteinases; proteases; urokinase; zymogen activation
资金
- Kommission Klinische Forschune der TU Munchen
- Bayerisch-Franzosisches Hochschulzentrum
Human kallikrein-related peptidases (KLKs) are 15 homologous serine proteases involved in several (patho)physiological processes, including cancer. Secreted as precursors, they are activated upon proteolytic release of a short propeptide. We searched for interconnection of KLKs within extracellular proteolytic networks leading to activation of protease zymogens and found that (i) pro-KLK activation by other KLKs is scarce, with the exception of pro-KLK which is efficiently activated by KLK4 and 5; (ii) pro-KLK4 is activated by matrix metalloproteinase 3; and (iii) trypsin-like KLKs efficiently activate the serine protease urokinase. Our observations provide new insights into the regulation of these important tumor-associated proteases.
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